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Recombinant human intrinsic factor is a glycoprotein produced using recombinant DNA technology in various expression systems (such as HEK293 cells[1], Sf9 insect cells[3], plants[7][8], and microalgae[10]). It mimics the naturally occurring gastric intrinsic factor secreted by parietal cells of the stomach. Its primary function is to bind vitamin B12 (cobalamin) in the gastrointestinal tract and facilitate its absorption in the terminal ileum via specific receptors. Recombinant forms are used for diagnostic purposes (e.g., as a reagent in immunoassays for anti-intrinsic factor antibodies), research applications related to vitamin B12 metabolism and absorption testing[4][6][7][8], and potentially therapeutic use to restore or enhance vitamin B12 uptake in patients with deficiency due to lack of endogenous intrinsic factor. The mechanism of action involves high-affinity binding to dietary vitamin B12 and subsequent receptor-mediated endocytosis into enterocytes.
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